Unspecific DNA binding of the DNA binding domain of the glucocorticoid receptor studied with flow linear dichroism

FEBS Letters

Nordén, Bengt²  Dahlman, Karin³  Carlstedt-Duke, Jan³  Hagmar, Per²  Gustafsson, Jan-Åke³  Takahashi, Masayuki¹ 

[1] Groupe de Cancérogenèse et de Mutagenése Moléculaire et Structurale, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15 rue René Descartes, F-670 84 Strasbourg cedex, France;Department of Physical Chemistry, Chalmers University of Technology, S-412 96 Gothenburg, Sweden;Department of Medical Nutrition and Center for Biotechnology, Karolinska Institute, Huddinge University Hospital, F82, S-141 86 Huddinge, Sweden

关键词: DNA-protein interaction;    Glucocorticoid receptor;    Linear dichroism;   

DOI  :  10.1016/0014-5793(89)80922-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The unspecific interaction between the DNA-binding domain of the human glucocorticoid receptor and DNA was studied using linear dichroism (LD) and circular dichroism (CD) spectroscopy. The amplitude of the LD signal was found to increase upon addition of protein at ionic strengths less than 60 nM Na⁺ indicating an increased persistence length of the complex compared to uncomplexed DNA. Analysis of the LD spectrum suggests that the binding does not involve intercalation of tyrosine residues. Evidence of saturation is found at a binding stoichiometry of approximately 5 DNA base pairs per protein monomer.

【 授权许可】

Unknown